GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR

Kim DH; Sarbassov DD; Ali SM; Latek RR; Guntur KVP; Erdjument-Bromage H; Tempst P; Sabatini DM · 2003 · Molecular Cell · Atlas ID KIM2003

Discovered mLST8 (GbetaL), the third core subunit that clamps onto mTOR's kinase domain and stabilizes the complex. It fine-tunes how tightly Raptor holds mTOR in response to nutrients - a small but essential cog that later proved especially critical for the mTORC2 complex.

At a glance

Evidence tierD Mechanistic / in vitro / review
Study type5 - Mechanistic / In Vitro
Model systemHuman cells (biochemistry)
JournalMolecular Cell
Year2003
Peer reviewedYes
SourceDOI 10.1016/s1097-2765(03)00114-x · PMID 12718876

Abstract

mTOR and raptor are components of a signaling pathway that regulates mammalian cell growth in response to nutrients and growth factors. Here, we identify a member of this pathway, a protein named GbetaL that binds to the kinase domain of mTOR and stabilizes the interaction of raptor with mTOR. Like mTOR and raptor, GbetaL participates in nutrient- and growth factor-mediated signaling to S6K1, a downstream effector of mTOR, and in the control of cell size. The binding of GbetaL to mTOR strongly stimulates the kinase activity of mTOR toward S6K1 and 4E-BP1, an effect reversed by the stable interaction of raptor with mTOR. Interestingly, nutrients and rapamycin regulate the association between mTOR and raptor only in complexes that also contain GbetaL. Thus, we propose that the opposing effects on mTOR activity of the GbetaL- and raptor-mediated interactions regulate the mTOR pathway.

Extracted findings

InterventionBiochemical – identification of GβL (mLST8)
TargetmTOR / raptor / GβL (mLST8)
ModelHuman cells (biochemistry)
EffectGβL binds the mTOR kinase domain and stabilizes the raptor–mTOR interaction; stimulates nutrient-sensitive signaling to S6K1 and cell-size control

Related topics

mTORC1mTORRaptormLST8

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